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. 1995 Sep 5;214(1):75-80.
doi: 10.1006/bbrc.1995.2258.

Cyclic GMP-mediated phospholamban phosphorylation in intact cardiomyocytes

B Sabine  1 , R Willenbrock, H Haase, P Karczewski, G Wallukat, R Dietz, E G Krause
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Cyclic GMP-mediated phospholamban phosphorylation in intact cardiomyocytes

B Sabine et al. Biochem Biophys Res Commun. .

Abstract

The cGMP-mediated phospholamban phosphorylation was investigated in cardiomyocytes in response to receptor-dependent (atrial natriuretic peptide, ANP) and -independent (sodium nitroprusside; SNP) cGMP generation. ANP (1 nM-1 microM) induced phospholamban phosphorylation in a concentration-dependent fashion (EC50: 5.0 +/- 0.09 nM). Concomitantly, an elevation in cGMP levels was observed. Phospholamban was also dose-dependently phosphorylated in response to SNP, but it required about three orders of magnitude higher concentrations (EC50: 2.9 +/- 0.03 microM) than ANP. Treatment of the cells with 8Br-cGMP (10 microM) or with the specific activator of cGMP-protein kinase 8-pCPT-cGMP (1-100 microM) mimicked these effects. The results demonstrate for the first time that a ANP/cGMP signaling pathway exists in neonatal cardiomyocytes which may contribute to modulation of heart contractility.

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